Characterization of specific p63 and p63-N-terminal isoform antibodies and their application for immunohistochemistry

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00209805%3A_____%2F13%3A%230000423" target="_blank" >RIV/00209805:_____/13:#0000423 - isvavai.cz</a>

Výsledek na webu

<a href="http://link.springer.com/article/10.1007%2Fs00428-013-1459-4" target="_blank" >http://link.springer.com/article/10.1007%2Fs00428-013-1459-4</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s00428-013-1459-4" target="_blank" >10.1007/s00428-013-1459-4</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Characterization of specific p63 and p63-N-terminal isoform antibodies and their application for immunohistochemistry

Popis výsledku v původním jazyce

The TP63 gene gives rise to protein isoforms with different properties and functions due to the presence (TAp63) or absence (?Np63) of N-terminal p53-like transactivation domain. Immunohistochemistry for p63 has clinical value for certain tumour types, but investigations have been hampered by a lack of well characterized antibodies and the inability to discriminate between these N-terminal isoforms with opposite functional properties. We have characterized a series of monoclonal antibodies to recombinant human TAp63 and two commercial p63 monoclonals by Western blot, immunostaining and phage display epitope mapping. 28 of 29 (96.6 %) novel monoclonals that recognized all p63 isoforms showed substantial cross-reactivity with p73, as did the commercial antibody, 4A4. One novel clone, PANp63-6.1, showed slight cross-reaction with p73 by Western blotting but not immunohistochemistry and the SFI-6 monoclonal did not cross-react with p73 or p53. Phage display revealed that PANp63-6.1 epitope

Název v anglickém jazyce

Characterization of specific p63 and p63-N-terminal isoform antibodies and their application for immunohistochemistry

Popis výsledku anglicky

The TP63 gene gives rise to protein isoforms with different properties and functions due to the presence (TAp63) or absence (?Np63) of N-terminal p53-like transactivation domain. Immunohistochemistry for p63 has clinical value for certain tumour types, but investigations have been hampered by a lack of well characterized antibodies and the inability to discriminate between these N-terminal isoforms with opposite functional properties. We have characterized a series of monoclonal antibodies to recombinant human TAp63 and two commercial p63 monoclonals by Western blot, immunostaining and phage display epitope mapping. 28 of 29 (96.6 %) novel monoclonals that recognized all p63 isoforms showed substantial cross-reactivity with p73, as did the commercial antibody, 4A4. One novel clone, PANp63-6.1, showed slight cross-reaction with p73 by Western blotting but not immunohistochemistry and the SFI-6 monoclonal did not cross-react with p73 or p53. Phage display revealed that PANp63-6.1 epitope

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EB - Genetika a molekulární biologie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2013

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Virchows Archiv

ISSN

0945-6317

e-ISSN

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Svazek periodika

463

Číslo periodika v rámci svazku

3

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

11

Strana od-do

415-425

Kód UT WoS článku

000323904700007

EID výsledku v databázi Scopus

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